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Lytic transglycosylases mitigate periplasmic crowding by degrading soluble cell wall turnover products
Weill Institute for Cell and Molecular Biology, Cornell University, NY, Ithaca, United States; Department of Microbiology, Cornell University, NY, Ithaca, United States.
Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).ORCID-id: 0000-0003-2429-7542
Weill Institute for Cell and Molecular Biology, Cornell University, NY, Ithaca, United States.
Weill Institute for Cell and Molecular Biology, Cornell University, NY, Ithaca, United States; Cornell Institute of Host-Microbe Interactions and Disease, Cornell University, NY, Ithaca, United States.
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2022 (Engelska)Ingår i: eLIFE, E-ISSN 2050-084X, Vol. 11, artikel-id e73178Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The peptidoglycan cell wall is a predominant structure of bacteria, determining cell shape and supporting survival in diverse conditions. Peptidoglycan is dynamic and requires regulated synthesis of new material, remodeling, and turnover – or autolysis – of old material. Despite exploitation of peptidoglycan synthesis as an antibiotic target, we lack a fundamental understanding of how peptidoglycan synthesis and autolysis intersect to maintain the cell wall. Here, we uncover a critical physiological role for a widely misunderstood class of autolytic enzymes, lytic transglycosylases (LTGs). We demonstrate that LTG activity is essential to survival by contributing to periplasmic processes upstream and independent of peptidoglycan recycling. Defects accumulate in Vibrio cholerae LTG mutants due to generally inadequate LTG activity, rather than absence of specific enzymes, and essential LTG activities are likely independent of protein-protein interactions, as heterologous expression of a non-native LTG rescues growth of a conditionally LTG-null mutant. Lastly, we demonstrate that soluble, uncrosslinked, endopeptidase-dependent peptidoglycan chains, also detected in the wild-type, are enriched in LTG mutants, and that LTG mutants are hypersusceptible to the production of diverse periplasmic polymers. Collectively, our results suggest that LTGs prevent toxic crowding of the periplasm with synthesis-derived peptidoglycan polymers and contrary to prevailing models, that this autolytic function can be temporally separate from peptidoglycan synthesis.

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eLife Sciences Publications Ltd , 2022. Vol. 11, artikel-id e73178
Nationell ämneskategori
Mikrobiologi inom det medicinska området
Identifikatorer
URN: urn:nbn:se:umu:diva-192274DOI: 10.7554/eLife.73178Scopus ID: 2-s2.0-85123743468OAI: oai:DiVA.org:umu-192274DiVA, id: diva2:1642268
Forskningsfinansiär
NIH (National Institute of Health), R01-GM130971Knut och Alice Wallenbergs Stiftelse, KAW2012.0184Vetenskapsrådet, VR2018-02823Kempestiftelserna, SMK2062NIH (National Institute of Health), R01-GM113172NIH (National Institute of Health), R35-GM136365Tillgänglig från: 2022-03-04 Skapad: 2022-03-04 Senast uppdaterad: 2022-10-31Bibliografiskt granskad

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Alvarez, Laura

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Alvarez, LauraCava, Felipe
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Molekylär Infektionsmedicin, Sverige (MIMS)Institutionen för molekylärbiologi (Medicinska fakulteten)
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Mikrobiologi inom det medicinska området

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